Gelation Properties Of Myofibrillar Protein Research Articles

Optimizing gelation properties of mixed meat myofibrillar proteins: investigating the effects of different proportions of beef, pork and chicken on physicochemical, structural and gelation properties.

The gelation properties of myofibrillar protein (MP) directly affect the texture, taste and water-holding capacity (WHC) of meat products. To enhance the gelation properties of single-species meat MP, the present study investigated the influence of different proportions of beef, pork and chicken MP on the physicochemical properties, structure and gelation properties of the MP. The results revealed that, when the proportion reached 5:2:3, the particle size decreases, leading to the maximum decomposition and unfolding of MPs, which exposes a greater number of hydrophobic amino acid residues. These changes promote interactions between protein molecules, especially the unfolding of α-helices and the formation of β-sheets during the heating process, which provides favorable conditions for the formation of protein gels and improves the gel strength and WHC of MP gels. Additionally, scanning electron microscopy revealed that the mixed MP gels are more compact and have more uniform gel networks and pores compared to single-species MP gels. Based on these results, the synergistic effect is induced by the interactions between proteins from different. This research provides a method for the subsequent development of new meat products and improvement of meat product quality, and also lays a theoretical foundation for composite research of proteins from different sources. © 2024 Society of Chemical Industry.

Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians)

Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m2/g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate–polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products.

Regulation mechanism of curcumin-loaded oil on the emulsification and gelation properties of myofibrillar protein: Emphasizing the dose-response of curcumin.

The regulation mechanism of curcumin (CUR) in the oil phase on the emulsification and gelation properties of myofibrillar protein (MP) was investigated. CUR enhanced the emulsifying activity index (EAI) of MP but decreased its turbiscan stability index (TSI) and surface hydrophobicity, which exacerbated oil droplet aggregation. Medium amounts (200mg/L) of CUR changed the 3D network architectures of emulsion gels from lamellar to reticular, improving the gels' water-holding capacity (WHC), storage modulus, springiness, and cohesiveness. Besides, the LF-NMR revealed that CUR had limited effects on the mobility of immobilized and free water. The α-helix of MP in gels with medium amounts of CUR decreased from 51% to 45%, but the β-sheet increased from 23% to 27% compared to those without CUR. Overall, CUR has the potential to become a novel structural modifier in emulsified meat products due to its dose-response.

Mechanism on the Synergistic Gelation of the Myofibrillar Protein Composite Gel Enhanced by "Clean-Label" Skin Functional Protein Powders.

The concept of healthiness and sustainability has promoted the innovation and development of "clean-label" products. Herein, this study aims to explore the influence mechanism of "clean label" skin protein powder (FPP) on the gelation properties of myofibrillar proteins (MPs). Specifically, the addition of FPP (0.2-4.0%) can improve the water holding capability and texture properties of MP composite gels. When the FPP concentration is over 1.0%, the composite gels exhibit no significant water loss during centrifugation. Dynamic rheology and sodium-dodecyl sulfate-polyacrylamide gel electrophoresis results revealed that FPP can slow the aggregation and denaturation of myosin and promote the formation of disulfide bonds between myofibril proteins, thus forming a stable network structure. Structural observation revealed that FPP can fill into the MP gel and lead to the formation of compact gel structures. Besides, with the increase of FPP concentration, the chemical forces involved in structural stabilization change significantly. Specifically, hydrophobic interaction and hydrogen bonding are the dominant forces at a lower FPP concentration (0.2 and 0.4%), while the ionic bond and disulfide bond are the dominant forces at a higher concentration. Overall, this work demonstrated that FPP can significantly improve the gel functionality of MP by altering the gel structure and strengthening the molecular forces.

Improvement of gelation properties of myofibrillar proteins from porcine longissimus dorsi muscle through microwave combined with air convection thawing treatment

Improvement of gelation properties of myofibrillar proteins from porcine longissimus dorsi muscle through microwave combined with air convection thawing treatment

Effects of NaCl on the interactions between neomethyl hesperidin dihydrochalcone and pork myofibrillar protein: Their relevance to gelation properties

Effects of sweetener neomethyl hesperidin dihydrochalcone (NHDC) on the gelation properties of myofibrillar protein (MP) at 0.2 M and 0.6 M NaCl were investigated. The results showed that addition of NHDC did not obviously change the cooking loss and strength of MP gels at 0.2 M NaCl. Whilst at 0.6 M NaCl, addition of high doses of NHDC (50–100 µM/g) remarkably increased cooking loss and decreased strength of MP gels. The expanded MP enhanced the interactions between NHDC and MP, leading to aggregation of MP as evidenced by the increasing particle size and the reducing solubility. The MP aggregates impeded hydrophobic interactions and disulfide bonds crosslinking in the gelation process, thereby damaged the gelation properties of MP at 0.6 M NaCl. This was supported by the poor network of MP gels observed by SEM. In the end, molecular docking elucidated the main types of interaction at molecular level, including hydrogen bonding and hydrophobicity. The results would provide guidance for NHDC as a potential sweetener in meat products.

Oxidative stability and gelation properties of myofibrillar protein from chicken breast after post-mortem frozen storage as influenced by phenolic compound-pterostilbene

The aim of this study was to elucidate the effects of dietary pterostilbene supplementation on physicochemical changes and gel properties of myofibrillar protein (MP) in chicken when subjected to short-term frozen storage. The results showed that pterostilbene supplementation diminished the oxidation of MP compared to the control, as the carbonyl content was significantly reduced and the loss of sulfhydryl and free amino groups was slowed. Meanwhile, the surface hydrophobicity and insolubility of MP were significantly reduced. FT-IR and endogenous fluorescence spectroscopy analysis indicated that dietary pterostilbene inhibited the unfolding of protein structure and the transition of α-helix to β-sheet structure. The integrity of the protein structure contributed to the gel quality. The strength, whiteness and water-holding capacity (WHC) of MP gels were improved in the pterostilbene treatment group. In terms of microstructure, pterostilbene facilitated the formation of dense and homogeneous gel network structure. In summary, these findings suggest that pterostilbene could be used as a dietary supplement to maintain the structural stability of MP in postmortem chicken breast muscle, allowing for excellent gel functional properties.

Effect of high pressure shucking on the gel properties and in vitro digestibility of myofibrillar proteins from red swamp crayfish (Procambarus clarkii)

The effect of high pressure shucking (HPS) on heat-induced gelation properties of myofibrillar proteins from shucked crayfish meat mince was investigated, by comparing with conventionally industrial shucking methods (i.e., freeze-thawing and cooking). The texture, color, water holding capacity, water distribution, microstructure, protein patterns and secondary structure as well as the pepsin digestibility and antioxidant activity of gels were evaluated. Compared to conventional shucking, HPS at 300 MPa resulted in good-quality gels with improved mechanical properties and desirable reddish color. The treatment seemed to be conducive to the maintenance of astaxanthin, although it slightly reduced the water holding capacity and proportion of T22 water. SEM analysis showed that the gels treated by HPS at 300 MPa had a more orderly and uniform microstructure with reduced pore size. Under this scenario, more myosin heavy chains appeared to be involved in the crosslinking as revealed by SDS-PAGE. However, FTIR results suggested that no obvious change was found in the protein secondary structure of gels. Intriguingly, HPS of 300 MPa enhanced the pepsin digestibility and ABTS-radical scavenging activity of the gels during in vitro digestion. These findings underlined the advantages of HPS for creating new gel-type products based on crayfish meat.

Properties of transglutaminase-induced myofibrillar/wheat gluten gels.

Gelation properties of myofibrillar protein (MP)/wheat gluten (WG) induced by glutamine transaminase (TGase) were studied. Results showed that the inclusion of transglutaminase increased the gel strength, water-holding capacity (WHC), and nonfreezable water (Wnf) of MP/WG mixture. Circular dichroism (CD) analysis showed that the β-sheet and random coil content of the MP/WG treated with TGase addition increased by 12.1% and 3.7%, while the α-helix and β-turn content decreased by 14.2% and 1.8%. Rheological measurements showed that TGase induced higher energy storage modulus value during the MP/WG gel heating-cooling cycle. the hydrogen bond and hydrophobic interaction content of the MP/WG gels increased by 80 and 120 ug/L, and the disulfide bond decreased by 200 ug/L, with TGase addition was increased from 0 to 120 U/g protein. Scanning electron microscope (SEM) showed that MP/WG gel with TGase had uniform and dense network structure. PRACTICAL APPLICATION: The properties of myofibrillar/wheat gluten gel induced by TGase crosslinking was studied. The gel structure and water holding capacity of MP/WG were improved by the cross-linking of TGase. The study of the gel properties of MP/WG induced by TGase crosslinking also can provide a theoretical basis for analyzing the effect of TGase on the application of gluten protein in complex meat emulsion system.

Gelation and microstructural properties of fish myofibrillar protein gels with the incorporation of l-lysine and l-arginine at low ionic strength.

The solubility limitation and poor gelation properties of myofibrillar proteins at low ionic strength are the most challenging obstacle to limit salt reduction in meat products. In the present study, five amino acids with different concentrations of 5, 10 15, and 20 mmol L-1 , l-lysine (Lys), l-arginine (Arg), l-histidine (His), l-proline (Pro) and l-glycine (Gly), were introduced into myofibrillar protein (MP) suspensions at low ionic strength to improve solubility and gelation properties. The dynamic rheological analysis showed that the MPs at 100 mmol L-1 NaCl containing 15/20 mmol L-1 Lys/Arg exhibited similar gelling behaviors to MPs at 600 mmol L-1 NaCl. Similarly, 15/20 mmol L-1 Lys/Arg significantly increased the solubility of MPs and the water holding capacity (WHC) and gel strength of MP gels, which was comparable to those of MPs at 600 mmol L-1 NaCl. Furthermore, Lys and Arg promoted the formation of aggregation-type gel with a dense and compact structure observed by scanning electron microscopy. The gels containing 15/20 mmol L-1 Lys/Arg exhibited a significant increase in the proportion of immobilized water (P21 ). The enhancement of WHC, gel strength, and P21 was closely associated with the increased solubility and the dense microstructure induced by Lys and Arg with high concentrations of 15 and 20 mmol L-1 . The knowledge obtained from this study may be useful for the improvement of gelation properties of MPs at low ionic strength using l-lysine and l-arginine. © 2021 Society of Chemical Industry.

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review.

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic-protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat-induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose-dependent and dual-role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross-linked three-dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

Effects of pulsed electric fields on the conformation and gelation properties of myofibrillar proteins isolated from pale, soft, exudative (PSE)-like chicken breast meat: A molecular dynamics study

The potential of pulsed electric field (PEF) of different intensities (8, 18, and 28 kV/cm) on the conformation and gelation properties of myofibrillar proteins (MPs) extracted from pale, soft, and exudative-like (PSE-like) chicken meat was investigated. The results showed a positive correlation between gelation properties and PEF intensities in the range of 8–18 kV/cm; however, a further increase in intensity had a negative impact. Optimized PEF treatment (18 kV/cm) was capable of inducing MPs with a relatively small particle size, thus contributing to the production of a more homogeneous gel structure. The water distribution and mobility in the gel system significantly changed with increasing PEF intensities, the proportion of immobilized water (P21) increased, and that of free water (P22) decreased. Based on molecular dynamics simulations (MDS), an increasing trend in the number of hydrogen bonds and a reduction in the radius of gyration (Rg) after PEF treatment.

The effects of three polysaccharides on the gelation properties of myofibrillar protein: Phase behaviour and moisture stability

The effects of three polysaccharides on the textural properties and microstructure of myofibrillar protein (MP) gels were studied. The gel strength and rheological properties of composite MP gels were significantly improved with insoluble dietary fibre (DF) and modified starch (MS) addition, while konjac glucomannan (KG) had limited effects at 1% addition. The SEM images indicated that moisture extrusion formed moisture channels and deteriorated the aggregation of MP gel networks during the thermal process. The polysaccharides stabilized moisture and reduced the appearance of moisture channels in the gel network, thereby promoting the formation of compact and integral gel networks. The MP-polysaccharide mixture is a thermally incompatible system and presented two main forms after the thermal process: 1) the “trapped” structure and 2) the “interpenetrated” structure. In the “trapped” structure, the MP was the dominant structure of the composite gel network. In the “interpenetrated” structure, the continuous polysaccharide hydrogel substantially hindered the aggregation of MP gel networks. Principal component analysis showed that the phase behaviour and moisture stability of polysaccharides significantly influenced the textural quality and microstructure of composite MP gelation. The study indicated that polysaccharides that contribute to moisture stability and form a “trapped structure” (phase behaviour) are ideal fat replacements for improving composite gel properties, especially DF.

The gelation properties of myofibrillar proteins prepared with malondialdehyde and (−)-epigallocatechin-3-gallate

Impact of malondialdehyde (MDA) and (−)-Epigallocatechin-3-gallate (EGCG) on gelling properties of myofibrillar proteins (MPs) was investigated. Addition of 6 mM MDA enhanced molecular interactions of proteins, thus the strength and elastic modulus (G′) of gel were improved. EGCG addition aggravated gel quality deterioration due to further modification of MPs induced by EGCG. Addition of 12 mM MDA jeopardized gel quality according to the increasing of strength and G′, but the decreasing of water-holding capacity (WHC), and the collapse of microstructure. Nevertheless, EGCG reacted with MDA forming EGCG-MDA adducts, hence improved gel quality, which was supported by the decreasing of strength, but the increasing of WHC, and the repaired microstructure of gel at 12 mM MDA. Addition of 24 mM MDA severely jeopardized gel quality, which became even worse due to EGCG addition. This work is helpful to understand the impact of MDA and polyphenols on the gel-forming capacity of MPs.

Assessment of structural, textural, and gelation properties of myofibrillar protein of silver carp (Hypophthalmichthys molitrix) modified by stunning and oxidative stress

This study aimed to investigate the effect of stunning and oxidative stress on gelation properties and water distribution of myofibrillar protein (MP) of silver carp fillets. Different stunning methods (percussion, ice/water, and gill cut) were conducted prior to in vitro MP oxidation by hydroxyl radicals generated from Fenton reaction (10 μM FeCl3, 0.1 mM ascorbic acid, and 0, 0.1, 0.5, 1, 5, and 10 mM H2O2) to simulate oxidative environments during surimi processing. The results indicated that gill cut-stunned fillets had greater susceptibility to MP unfolding and oxidation in terms of elevated disulfide bonds, carbonyls, and surface hydrophobicity. Regardless of stunning stress, mild oxidative modifications (0.1–1 mM H2O2) facilitated the enhancement of gel-forming ability, while strong oxidative environments (5–10 mM H2O2) exhibited weakened gel strength with reduced textural properties. In addition, gill cut-stunned fillets showed higher free water content (16.73%) and attenuated gel strength (278.12 g mm), reflecting fragile gel network and poor water-holding capacity in oxidized MP gels. In conclusion, gill cut stunning were not recommended in aquatic processing in terms of inferior water retention and decreased deformation and springiness of gels.

Effects of partial substitution of NaCl on gel properties of fish myofibrillar protein during heating treatment mediated by microbial transglutaminase

The effects of partial substitution of NaCl with KCl, MgCl2 and CaCl2 on gelation properties of myofibrillar protein (MP) mediated by microbial transglutaminase during the heating process were studied, including texture, color, water-holding capacity, rheological properties, Raman spectra and microstructure. Ranking of chlorinated salts efficiency showed NaCl > KCl > MgCl2 > CaCl2. The NaCl and KCl groups of MP gels exhibited similar water-holding capacity and gel strength. The gel strength was all decreased in the MP gels containing KCl, CaCl2 and MgCl2 compared to the NaCl group, while the KCl group reduced the gel strength to a less extent. The rheological properties of NaCl and KCl groups showed significant higher G′ and G″ values compared to the control group. Thus, the utilization of chlorinated salts substitutes is a promising way to reduce sodium content in fish products. These results could be used for references in developing low-sodium meat and fish products.

Gelling properties of myofibrillar protein from abalone (Haliotis Discus Hannai Ino) muscle

ABSTRACTTexture of muscle food is dependent on the gelation properties of myofibrillar protein. Defining the performance of myofibrillar protein during gelation is beneficial for maintaining quality and developing muscle food. The myofibrillar protein from abalone muscle (AMP) was extracted and the gel-forming ability was investigated. The lowest protein solubility of AMP in distilled water was obtained at pH 5.5, but shifted to a lower pH value by ionic strength. The breaking force and deformation of AMP gel formed at pH 7.0 were 48.00 g and 27.70 mm, respectively, but they could not be detected at pH 5.0 and pH 5.5 due to the low gel-forming ability. Scanning electron microscopy data showed that a coarse and disorder gel containing clusters of agglomerates was observed at pH 5.0 and pH 5.5, but gradual compact network structure was observed in the gel formed at increasing pH. The glass transition temperature (Tg) of AMP gel formed at pH 5.5 was higher than that of AMP, and the Tg of AMP gel was increased with increasing the pH of gel-forming solution. It was found that the unfolding of tertiary structure of AMP at pH 7.0 was easier than that at pH 5.5 through the result of infrared spectra. We therefore conclude that both the solubility and gel-forming ability of AMP are pH dependent.

Effects of vacuum chopping on physicochemical and gelation properties of myofibrillar proteins from silver carp (Hypophthalmichthys molitrix)

Physicochemical and gelation properties of myofibrillar proteins from silver carp surimi as affected by chopping under different vacuum degrees (0, 0.01, 0.02, 0.04, 0.06 and 0.08 MPa) were investigated. With the increase of vacuum degree, size and quantity of air bubbles in surimi paste decreased, disulfide bond content of myofibrillar proteins decreased significantly (p < .05) and then slight increased (p > .05), while surface hydrophobicity of myofibrillar proteins increased gradually (p < .05). Gel mechanical properties, chemical interactions (nonspecific associations, hydrogen bond and hydrophobic interactions) and FAXL (cross-linking degree of free amino group) of heat-induced surimi gel increased significantly (p < .05) with vacuum degree. Scanning electron microscopy (SEM) observation showed that three-dimensional network of surimi gel under higher vacuum degree was more compact and orderly. Results indicated that vacuum chopping imparted physicochemical and structural changes of fish myofibrillar protein, which might contribute to the improvement in gelling properties of myofibrillar proteins.

Controlled Cross-Linking with Glucose Oxidase for the Enhancement of Gelling Potential of Pork Myofibrillar Protein.

Differential oxidative modifications of myofibrillar protein (MP) by hydroxyl radicals generated in an enzymatic system with glucose oxidase (GluOx) in the presence of glucose/FeSO4 versus a Fenton system (H2O2/FeSO4) were investigated. Pork MP was modified at 4 °C and pH 6.25 with hydroxyl radicals produced from 1 mg/mL glucose in the presence of 80, 160, or 320 μg/mL GluOx and 10 μM FeSO4. Total sulfhydryl content, solubility, cross-linking pattern, and gelation properties of MP were measured. H2O2 production proceeded linearly with the concentration of GluOx and increased with reaction time. GluOx- and H2O2-dose-dependent protein polymerization, evidenced by faded myosin heavy chain and actin in SDS-PAGE as well as significant decreases in sulfhydryls, coincided with protein solubility loss. Firmer and more elastic MP gels were produced by GluOx than by the Fenton system at comparable H2O2 levels due to an altered radical reaction pathway.

Effects of high pressure modification on conformation and gelation properties of myofibrillar protein

The effects of high pressure (HP) treatment (100–500MPa) on conformation and gelation properties of myofibrillar protein (MP) were investigated. As pressure increased (0.1–500MPa), α-helix and β-sheet changed into random coil and β-turn, proteins unfolded to expose interior hydrophobic and sulfhydryl groups, therefore surface hydrophobicity and formation of disulfide bonds were strengthened. At 200MPa, protein solubility and gel hardness reached their maximum value, particle size had minimum value, and gel microstructure was dense and uniform. DSC data showed that actin and myosin completely denatured at 300MPa and 400MPa, respectively. Rheological modulus (G′ and G″) of HP-treated MP decreased as pressure increased during thermal gelation. Moderate HP treatment (≦200MPa) strengthened gelation properties of MP, while stronger HP treatment (⩾300MPa) weakened the gelation properties. 200MPa was the optimum pressure level for modifying MP conformation to improve its gelation properties.